A beta-turn rich barley seed protein is correctly folded in Escherichia coli.
Protein Expr Purif
; 5(4): 357-63, 1994 Aug.
Article
em En
| MEDLINE
| ID: mdl-7950382
Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (> or = 30mg/liter). N-terminal sequence analysis, SDS-PAGE, RP-HPLC, cd spectroscopy, and small angle X-ray scattering demonstrated that their physicochemical properties were similar to those of C hordeins isolated from barley grain. This indicates that the expressed proteins were correctly folded. The cysteine-containing mutant showed evidence of polymer formation in E. coli, nonreduced preparations of the protein showing the presence of polymers that were replaced by a single protein when a reducing agent was added.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Hordeum
/
Estrutura Secundária de Proteína
/
Dobramento de Proteína
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article